Photoaffinity labeling of an herbicide receptor protein in chloroplast membranes
AUTOR(ES)
Pfister, Klaus
RESUMO
2-Azido-4-ethylamino-6-isopropylamino-s-triazine (azido-atrazine) inhibits photosynthetic electron transport at a site identical to that affected by atrazine (2-chloro-4-ethylamino-6-isopropylamino-s-triazine). The latter is a well-characterized inhibitor of photosystem II reactions. Azido-atrazine was used as a photoaffinity label to identify the herbicide receptor protein; UV irradiation of chloroplast thylakoids in the presence of azido[14C]atrazine resulted in the covalent attachment of radioactive inhibitor to thylakoid membranes isolated from pea seedlings and from a triazine-susceptible biotype of the weed Amaranthus hybridus. No covalent binding of azido-atrazine was observed for thylakoid membranes isolated from a naturally occurring triazine-resistant biotype of A. hybridus. Analysis of thylakoid polypeptides from both the susceptible and resistant A. hybridus biotypes by sodium dodecyl sulfate/polyacrylamide gel electrophoresis, followed by fluorography to locate 14C label, demonstrated specific association of the azido[14C]atrazine with polypeptides of the 34- to 32-kilodalton size class in susceptible but not in resistant membranes.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=319929Documentos Relacionados
- Photo-Affinity Labeling of Specific Acetylcholine-Binding Sites on Membranes
- Photoaffinity labeling of rat androgen binding protein.
- Photoaffinity labeling of Torpedo acetylcholine receptor at multiple sites.
- Macromolecular photoaffinity labeling of the lutropin receptor on granulosa cells.
- Identification and characterization of the ecdysterone receptor in Drosophila melanogaster by photoaffinity labeling
